MolNFT v1 · #165242 · protein
Structure of the pore C-terminal domain, a protein of T9SS from porphyromonas gingivalis
6TOP: “Structure of the pore C-terminal domain, a protein of T9SS from porphyromonas gingivalis”. X-ray diffraction, 2 ligands (MLD, NA). MolNFT v1 #165242 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6TOP
- Type
- protein
- Length
- 606 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- T2NEY1
- Ligands
- MLD, NA
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 155 | — | T2NEY1 |
| B, C | — | protein | 150 | — | T2NEY1 |
| D | — | protein | 151 | — | T2NEY1 |
Ligands and binding sites
- MLD · Glcnac(beta1-4)-murnac(1,6-anhydro)-L-ala-gamma-D-glu-meso-A2PM-D-ala · ligand · 2 copies · chains B, C
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6TOP · Structure of the PorE C-terminal domain, a protein of T9SS from Porphyromonas gingivalis · the same entry in another collection · chain B against B, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt T2NEY1
- Elsewhere: RCSB PDB 6TOP · PDBe 6TOP · UniProt T2NEY1
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